Structure and mechanism of mouse cysteine dioxygenase.

Abstract:

:Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme.

authors

McCoy JG,Bailey LJ,Bitto E,Bingman CA,Aceti DJ,Fox BG,Phillips GN Jr

doi

10.1073/pnas.0509262103

keywords:

subject

Has Abstract

pub_date

2006-02-28 00:00:00

pages

3084-9

issue

9

eissn

0027-8424

issn

1091-6490

pii

0509262103

journal_volume

103

pub_type

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